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TitleConformational landscape of soluble α-klotho revealed by cryogenic electron microscopy.
Journal, issue, pagesSci Rep, Vol. 15, Issue 1, Page 543, Year 2025
Publish dateJan 2, 2025
AuthorsNicholas J Schnicker / Zhen Xu / Mohammad Amir / Lokesh Gakhar / Chou-Long Huang /
PubMed Abstractα-Klotho (KLA) is a type-1 membranous protein that can associate with fibroblast growth factor receptor (FGFR) to form co-receptor for FGF23. The ectodomain of unassociated KLA is shed as soluble ...α-Klotho (KLA) is a type-1 membranous protein that can associate with fibroblast growth factor receptor (FGFR) to form co-receptor for FGF23. The ectodomain of unassociated KLA is shed as soluble KLA (sKLA) to exert FGFR/FGF23-independent pleiotropic functions. The previously determined X-ray crystal structure of the extracellular region of sKLA in complex with FGF23 and FGFR1c suggests that sKLA functions solely as an on-demand coreceptor for FGF23. To understand the FGFR/FGF23-independent pleiotropic functions of sKLA, we investigated biophysical properties and structure of apo-sKLA. Single particle cryogenic electron microscopy (cryo-EM) revealed a 3.3 Å resolution structure of apo-sKLA that overlays well with its counterpart in the ternary complex with several distinct features. Compared to the ternary complex, the KL2 domain of apo-sKLA is more flexible. Three-dimensional variability analysis revealed that apo-sKLA adopts conformations with different KL1-KL2 interdomain bending and rotational angles. Mass photometry revealed that sKLA can form a stable structure with FGFR and/or FGF23 as well as sKLA dimer in solution. Cryo-EM supported the dimeric structure of sKLA. Recent studies revealed that FGF23 contains two KLA-binding sites. Our computational studies revealed that each site binds separate KLA in the dimer. The potential multiple forms and shapes of sKLA support its role as FGFR-independent hormone with pleiotropic functions. The ability of FGF23 to engage two KLA's simultaneously raises a potential new mechanism of action for FGF23-mediated signaling by the membranous klotho.
External linksSci Rep / PubMed:39747283 / PubMed Central
MethodsEM (single particle)
Resolution3.29 - 6.5 Å
Structure data

41452

8toh

EMDB-41452, PDB-8toh:
Cryo-EM structure of monomeric alpha-Klotho
Method: EM (single particle) / Resolution: 3.29 Å

42186

8uf8

EMDB-42186, PDB-8uf8:
Cryo-EM structure of alpha-Klotho
Method: EM (single particle) / Resolution: 6.5 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / protein binding

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